Human platelets were extracted with acid-ethanol and platelet-derived TGF-beta was purified from the extract by a two-column procedure using sequential gel filtration in the absence and then presence of urea. Purified TGF-beta is a protein of 25,000-daltons, and it is comprised of two 12,500-dalton subunits held together by disulfide bonds. The purified factor elicits its biological activity at concentrations less than 4pM. Comparative studies showed that platelets contain 100 times more TGF-beta than do other non-neoplastic tissues. Incubation of TGF-beta with NRK cells results in an increased number of cell surfaced EGF receptors. IGF-II receptors are not affected.